scholarly journals Fibronectin Fragment Activation of Proline-rich Tyrosine Kinase PYK2 Mediates Integrin Signals Regulating Collagenase-3 Expression by Human Chondrocytes through a Protein Kinase C-dependent Pathway

2003 ◽  
Vol 278 (27) ◽  
pp. 24577-24585 ◽  
Author(s):  
Richard F. Loeser ◽  
Christopher B. Forsyth ◽  
Allen M. Samarel ◽  
Hee-Jeong Im
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Human Chondrocytes ◽  
Kinase C ◽  
Fibronectin Fragment ◽  
Dependent Pathway

scholarly journals Erythropoietin increases c-myc mRNA by a protein kinase C-dependent pathway.

1991 ◽  
Vol 266 (2) ◽  
pp. 681-684 ◽  
Author(s):  
R Spangler ◽  
S C Bailey ◽  
A J Sytkowski
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Dependent Pathway

scholarly journals Role of tyrosine kinase and protein kinase C in the steroidogenic actions of angiotensin II, α-melanocyte-stimulating hormone and corticotropin in the rat adrenal cortex

1995 ◽  
Vol 305 (2) ◽  
pp. 433-438 ◽  
Author(s):  
S Kapas ◽  
A Purbrick ◽  
J P Hinson
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Zona Glomerulosa ◽  
Aldosterone Secretion ◽  
Melanocyte Stimulating Hormone ◽  
Kinase C ◽  
Stimulating Hormone

The role of protein kinases in the steroidogenic actions of alpha-melanocyte-stimulating hormone (alpha-MSH), angiotensin II (AngII) and corticotropin (ACTH) in the rat adrenal zona glomerulosa was examined. Ro31-8220, a potent selective inhibitor of protein kinase C (PKC), inhibited both AngII- and alpha-MSH-stimulated aldosterone secretion but had no effect on aldosterone secretion in response to ACTH. The effect of Ro31-8220 on PKC activity was measured in subcellular fractions. Basal PKC activity was higher in cytosol than in membrane or nuclear fractions. Incubation of the zona glomerulosa with either alpha-MSH or AngII resulted in significant increases in PKC activity in the nuclear and cytosolic fractions and decreases in the membrane fraction. These effects were all inhibited by Ro31-8220. ACTH caused a significant increase in nuclear PKC activity only, and this was inhibited by Ro31-8220 without any significant effect on the steroidogenic response to ACTH, suggesting that PKC translocation in response to ACTH may be involved in another aspect of adrenal cellular function. Tyrosine phosphorylation has not previously been considered to be an important component of the response of adrenocortical cells to peptide hormones. Both AngII and alpha-MSH were found to activate tyrosine kinase, but ACTH had no effect, observations that have not been previously reported. Tyrphostin 23, a specific antagonist of tyrosine kinases, inhibited aldosterone secretion in response to AngII and alpha-MSH, but not ACTH. These data confirm the importance of PKC in the adrenocortical response to AngII and alpha-MSH, and, furthermore, indicate that tyrosine kinase may play a critical role in the steroidogenic actions of AngII and alpha-MSH in the rat adrenal zona glomerulosa.

Arginine-Vasopressin Stimulates CRH and ACTH Release by Rat Adrenal Medulla, Acting Via the V 1 Receptor Subtype and a Protein Kinase C-Dependent Pathway

Peptides ◽  
1997 ◽  
Vol 18 (2) ◽  
pp. 191-195 ◽  
Author(s):  
Giuseppina Mazzocchi ◽  
Ludwik K Malendowicz ◽  
Pierra Rebuffat ◽  
Cinzia Tortorella ◽  
Gastone G Nussdorfer
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Adrenal Medulla ◽  
Arginine Vasopressin ◽  
Receptor Subtype ◽  
Kinase C ◽  
Dependent Pathway ◽  
Acth Release
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